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Biochem Biophys Res Commun. 1994 Feb 15;198(3):1113-8.

Molecular cloning and functional expression of a human peroxisomal acyl-coenzyme A oxidase.

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Department of Biochemistry, Shinshu University School of Medicine, Nagano, Japan.


cDNA encoding the human peroxisomal acyl-coenzyme A oxidase (AOX) was cloned and sequenced. The longest cDNA insert isolated has 3083 bases and encodes the entire protein of 661-amino acids, including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal. At the amino acid level, the significantly high homology (89%) to rat AOX was found. In the cDNA-expression experiment, significant amount of AOX was accumulated in human skin fibroblast and the expressed AOX was catalytically active, while only a limited amount was found in Zellweger syndrome patient's fibroblast not having normal peroxisomes.

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